Loading…
A polyalanine peptide derived from polar fish with anti-infectious activities
Due to the growing concern about antibiotic-resistant microbial infections, increasing support has been given to new drug discovery programs. A promising alternative to counter bacterial infections includes the antimicrobial peptides (AMPs), which have emerged as model molecules for rational design...
Saved in:
Published in: | Scientific reports 2016-02, Vol.6 (1), p.21385-21385, Article 21385 |
---|---|
Main Authors: | , , , , , , , , , , , |
Format: | Article |
Language: | English |
Subjects: | |
Citations: | Items that this one cites Items that cite this one |
Online Access: | Get full text |
Tags: |
Add Tag
No Tags, Be the first to tag this record!
|
Summary: | Due to the growing concern about antibiotic-resistant microbial infections, increasing support has been given to new drug discovery programs. A promising alternative to counter bacterial infections includes the antimicrobial peptides (AMPs), which have emerged as model molecules for rational design strategies. Here we focused on the study of
Pa
-MAP 1.9, a rationally designed AMP derived from the polar fish
Pleuronectes americanus
.
Pa
-MAP 1.9 was active against Gram-negative planktonic bacteria and biofilms, without being cytotoxic to mammalian cells. By using AFM, leakage assays, CD spectroscopy and
in silico
tools, we found that
Pa
-MAP 1.9 may be acting both on intracellular targets and on the bacterial surface, also being more efficient at interacting with anionic LUVs mimicking Gram-negative bacterial surface, where this peptide adopts α-helical conformations, than cholesterol-enriched LUVs mimicking mammalian cells. Thus, as bacteria present varied physiological features that favor antibiotic-resistance,
Pa
-MAP 1.9 could be a promising candidate in the development of tools against infections caused by pathogenic bacteria. |
---|---|
ISSN: | 2045-2322 2045-2322 |
DOI: | 10.1038/srep21385 |